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A broad-spectrum chemokine antagonist encoded by Kaposi's sarcoma-associated herpesvirus.

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Affiliations

  • 1. Laboratory for Molecular Pharmacology, Institute of Pharmacology, Panum Institute, University of Copenhagen, DK-2200 Copenhagen, Denmark.
      Authors
    • Kledal TN 1
    (1 author)

ORCIDs linked to this article

Science, 01 Sep 1997, 277(5332):1656-1659
https://doi.org/10.1126/science.277.5332.1656 PMID: 9287217 

Abstract 

Kaposi's sarcoma-associated herpesvirus encodes a chemokine called vMIP-II. This protein displayed a broader spectrum of receptor activities than any mammalian chemokine as it bound with high affinity to a number of both CC and CXC chemokine receptors. Binding of vMIP-II, however, was not associated with the normal, rapid mobilization of calcium from intracellular stores; instead, it blocked calcium mobilization induced by endogenous chemokines. In freshly isolated human monocytes the virally encoded vMIP-II acted as a potent and efficient antagonist of chemotaxis induced by chemokines. Because vMIP-II could inhibit cell entry of human immunodeficiency virus (HIV) mediated through CCR3 and CCR5 as well as CXCR4, this protein may serve as a lead for development of broad-spectrum anti-HIV agents.

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Read article at publisher's site: https://doi.org/10.1126/science.277.5332.1656

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